Q9LU02 · BGL13_ARATH
- ProteinBeta-glucosidase 13
- GeneBGLU13
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids507 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
Catalytic activity
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 50 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 154 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 199-200 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: NE | ||||||
Active site | 200 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 344 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Active site | 414 | Nucleophile | ||||
Sequence: E | ||||||
Binding site | 414 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 459 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 466-467 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: EW | ||||||
Binding site | 475 | a beta-D-glucoside (UniProtKB | ChEBI) | ||||
Sequence: F |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Molecular Function | beta-glucosidase activity | |
Molecular Function | scopolin beta-glucosidase activity | |
Biological Process | carbohydrate metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBeta-glucosidase 13
- EC number
- Short namesAtBGLU13
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9LU02
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MRTKYFSLLVFIIVLASNEVIA | ||||||
Chain | PRO_0000389576 | 23-507 | Beta-glucosidase 13 | |||
Sequence: KKHSSTPKLRRSDFPKDFIFGAATSAYQVEGAAHEDGRGPSIWDTFSEKYPEKIKDGTNGSIASDSYHLYKEDVGLLHQIGFGAYRFSISWSRILPRGNLKGGINQAGIDYYNNLINELLSKGIKPFATIFHWDTPQSLEDAYGGFFGAEIVNDFRDYADICFKNFGDRVKHWMTLNEPLTVVQQGYVAGVMAPGRCSKFTNPNCTAGNGATEPYIVGHNLILAHGEAVKVYREKYKASQKGQVGIALNAGWNLPYTESAEDRLAAARAMAFTFDYFMEPLVTGKYPVDMVNNVKDGRLPTFTAKQSKMLKGSYDFIGINYYSSSYAKDVPCSSENVTLFSDPCASVTGEREGVPIGPKAASDWLLIYPKGIRDLLLYAKYKFKDPVMYITENGRDEASTGKIDLKDSERIDYYAQHLKMVQDAISIGANVKGFFAWSLLDNFEWATGYSVRFGLVYVDFNDGRKRYPKKSAKWFRKLLSEKKRN | ||||||
Glycosylation | 81 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 219↔227 | |||||
Sequence: CSKFTNPNC | ||||||
Glycosylation | 226 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 358 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length507
- Mass (Da)56,957
- Last updated2000-10-01 v1
- Checksum83AC8DC0DC7AC434
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB024024 EMBL· GenBank· DDBJ | BAA98117.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED95142.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT033043 EMBL· GenBank· DDBJ | ACE79745.1 EMBL· GenBank· DDBJ | mRNA |